Effect of IgG-horseradish peroxidase conjugates purified on Con A-Sepharose upon sensitivity of enzyme immunoassay.
Antibodies coupled to horseradish peroxidase (HRP) were purified by gel filtration and by combination of affinity chromatography and gel filtration. Binding kinetics to solid phase bound antigens were studied of the antibody-enzyme conjugates in the presence and in the absence of unlabelled IgG. The detection limit in enzyme immunoassay was found to be lowered by factor 16 after elimination of unlabelled IgG from the conjugate.
D000818:Animals; D000906:Antibodies; D003208:Concanavalin A; D006168:Guinea Pigs; D006514:Hepatitis B Surface Antigens / Q000032:analysis*; D006735:Horseradish Peroxidase; D005779:Immunodiffusion / Q000379:methods; D007124:Immunoenzyme Techniques; D007074:Immunoglobulin G; D007700:Kinetics; D008832:Microchemistry; D010544:Peroxidases; D011134:Polysaccharides; D012685:Sepharose
D000906:Antibodies; D006514:Hepatitis B Surface Antigens; D007074:Immunoglobulin G; D011134:Polysaccharides; D003208:Concanavalin A; D012685:Sepharose; D006735:Horseradish Peroxidase; D010544:Peroxidases